Evidence map›Paper›PMID 29728914›Full record

ArticleAmino acids2018

Prediction and characterization of a novel hemocyanin-derived antimicrobial peptide from shrimp Litopenaeus vannamei.

Shen Yang, He Huang, Fan Wang, Jude Juventus Aweya, Zhihong Zheng, Yueling Zhang

Open access · hybridAbstract read
In one paragraph

Article in Amino acids, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing papers in PubMed
2.6field-weighted citation impact, top 10% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

17 citing papers in PubMed, 50 citations in OpenAlex.

  1. Review
  2. Frontiers in microbiology · 2026
    Article
  3. Review
  4. Review
  5. Article
  6. Article
  7. Antibacterial Action of Protein Fraction Isolated fromPharmaceuticals (Basel, Switzerland) · 2024
    Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Article
  15. Article
  16. Collection of antimicrobial peptides database and its derivatives: Applications and beyond.Protein science : a publication of the Protein Society · 2020
    Article
  17. AMolecules (Basel, Switzerland) · 2018
    Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Shen YangDepartment of Biology and Guangdong Provincial Key Laboratory of Marine Biotechnology, School of Science, Shantou University, Shantou, 515063, Guangdong, China.
He HuangDepartment of Biology and Guangdong Provincial Key Laboratory of Marine Biotechnology, School of Science, Shantou University, Shantou, 515063, Guangdong, China.
Fan WangDepartment of Biology and Guangdong Provincial Key Laboratory of Marine Biotechnology, School of Science, Shantou University, Shantou, 515063, Guangdong, China.
Jude Juventus AweyaDepartment of Biology and Guangdong Provincial Key Laboratory of Marine Biotechnology, School of Science, Shantou University, Shantou, 515063, Guangdong, China.
Zhihong ZhengDepartment of Biology and Guangdong Provincial Key Laboratory of Marine Biotechnology, School of Science, Shantou University, Shantou, 515063, Guangdong, China.
Yueling ZhangDepartment of Biology and Guangdong Provincial Key Laboratory of Marine Biotechnology, School of Science, Shantou University, Shantou, 515063, Guangdong, China. zhangyl@stu.edu.cn.ORCID http://orcid.org/0000-0002-0510-8307
Shantou University · CN

Funding

National Natural Science Foundation of China 31372558National Natural Science Foundation of China 31672689Natural Science Foundation of Guangdong Province 2017A030311032
6 · The paper itself

Abstract

Hemocyanin, the multifunctional glycoprotein in the hemolymph of invertebrates, can generate various antimicrobial peptides (AMPs). Given the rising interest in the use of natural therapeutic agents such as AMPs, alternative and more efficient methods for their generation are being explored. In this work, free online software was first applied to predict the generation of antimicrobial peptides from the large subunit of Litopenaeus vannamei hemocyanin. Twenty potential antimicrobial peptides ranging from 1.5 to 1.9 kDa were predicted, five of which had α-helical structures and were selected for antibacterial activity testing. The results indicated that these five peptides had antibacterial activity against seven different bacteria. Of the five peptides, one peptide, designated L1, had the strongest antibacterial activity against both Gram-negative and Gram-positive bacteria. Moreover, CD and NMR data showed that L1 had both α-helical and β-turns structural composition, and that these structures were essential for L1's antibacterial activity. Furthermore, SEM analysis revealed that peptide L1 had broad-spectrum activity against both Gram-positive and Gram-negative bacteria, as it could destroy the bacterial cell walls and kill the bacteria. Thus, L1 is a very potent antimicrobial peptide that can be exploited and used in antibacterial therapeutics.

Indexed as

Anti-Bacterial AgentsCrustaceaPeptidesAnimalsBacteriaHemocyaninsHemolymphAnti-Bacterial AgentsHemocyaninsPeptidesAntimicrobial peptideHemocyaninLitopenaeus vannameiPrediction

Identifiers

PMID29728914
PMCPMC6060862
OpenAlexW2800263663

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.